| pubmed-article:91652 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:91652 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:91652 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
| pubmed-article:91652 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:91652 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:91652 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:91652 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:91652 | pubmed:dateCreated | 1980-1-19 | lld:pubmed |
| pubmed-article:91652 | pubmed:abstractText | A selectively Fc gamma-binding protein was isolated from purified and radioiodinated cell membranes from two cases of B-type chronic lymphocytic leukemia and one case of B-type prolymphocytic leukemia by binding to IgG aggregates, horseradish peroxidase-anti-peroxidase IgG complexes, and sheep erythrocyte membrane sheets densely coated with IgG. This protein could not be isolated from the cell membranes of an Fc gamma-receptor-negative chronic lymphocytic leukemia of the T type or from membranes of human erythrocytes. The Fc gamma-binding protein was efficiently solubilized by a mixture of Na-EDTA and 2-mercaptoethanol, but not with one of these agents alone, indicating that both divalent cations and disulfide bridges are involved in the linkage of the Fc gamma-binding protein to the cell membrane. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the Fc gamma-binding protein revealed an apparent mol wt of 28,000 and in isoelectric focusing it showed an isoelectric point of 5.5. The electrophoretic mobility of the 28,000-dalton protein did not change after reduction and alkylation. It was determined that the NH2-terminal amino acid of the protein was glycine. The isolated protein was unable to agglutinate antibody-coated erythrocytes. These findings suggest that the 28,000-dalton IgG-affined protein was composed to O2-enriched buffer lacking reducing agents, the 28,000-dalton protein aggregated to a 115,000-dalton molecule. The isolated Fc gamma-binding protein proved to be different from C1q or its subunits. | lld:pubmed |
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| pubmed-article:91652 | pubmed:language | eng | lld:pubmed |
| pubmed-article:91652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:91652 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:91652 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:91652 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:91652 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:91652 | pubmed:author | pubmed-author:SteinHH | lld:pubmed |
| pubmed-article:91652 | pubmed:author | pubmed-author:ThoenesJJ | lld:pubmed |
| pubmed-article:91652 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:91652 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:91652 | pubmed:volume | 150 | lld:pubmed |
| pubmed-article:91652 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:91652 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:91652 | pubmed:pagination | 1049-66 | lld:pubmed |
| pubmed-article:91652 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:91652 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:91652 | pubmed:articleTitle | Properties of an Fc gamma-binding protein isolated from human leukemic B cells. | lld:pubmed |
| pubmed-article:91652 | pubmed:publicationType | Journal Article | lld:pubmed |
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